A comparison of the glutathione S-transferases of trout and rat liver

1979 ◽  
Vol 63 (3) ◽  
pp. 423-427 ◽  
Author(s):  
I.A. Nimmo ◽  
J.B. Clapp ◽  
R.C. Strange
Keyword(s):  
Rat Liver ◽  
Glutathione S Transferases

scholarly journals Studies on the subunit composition of rat liver glutathione S-transferases.

1983 ◽  
Vol 258 (18) ◽  
pp. 11321-11325 ◽  
Author(s):  
A B Frey ◽  
T Friedberg ◽  
F Oesch ◽  
G Kreibich
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases

Subunit composition of rat liver glutathione S-transferases

1982 ◽  
Vol 108 (2) ◽  
pp. 461-467 ◽  
Author(s):  
Chen-Pei D. Tu ◽  
Mitchell J. Weiss ◽  
C. Channa Reddy
Keyword(s):  
Rat Liver ◽  
Subunit Composition ◽  
Liver Glutathione ◽  
Glutathione S Transferases

scholarly journals Inhibition by inorganic anions of glutathione S-transferases from insect and mammalian sources

1991 ◽  
Vol 278 (1) ◽  
pp. 193-198 ◽  
Author(s):  
A G Clark ◽  
J F Hamilton ◽  
S N Marshall
Keyword(s):  
Rat Liver ◽  
Galleria Mellonella ◽  
Limited Range ◽  
Inorganic Anions ◽  
Glutathione S Transferase ◽  
Inhibitory Potency ◽  
Glutathione S Transferases ◽  
Wax Moth

Glutathione S-transferases 1-1, 3-3, 3-4 and 4-4 from rat liver and the major glutathione S-transferase from the wax moth (Galleria mellonella) are all inhibited by several simple inorganic anions. For each of 3-3, 3-4 and the insect enzyme, the order of inhibitory potency was ClO4- greater than or equal to SCN- greater than I- greater than NO3- greater than Br-. A more limited range of anions was tested on the isoenzymes 1-1 and 4-4, but the same trend was apparent. Values for Ki ranged from about 200 mM for Cl- to 6 mM for SCN- in the case of the insect enzyme and from 50 mM for Br- to 0.3 mM for SCN- for the rat isoform 3-3. Acetate, F-, SO4(2-) and PO4(3-) were not found to have significant inhibitory properties. The mode of inhibition was characterized as non-competitive in the case of the insect enzyme and rat transferase 1-1, whereas the mode of inhibition was partially non-competitive in the case of the rat isoforms 3-3, 3-4 and 4-4.

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